Post-translational modifications such as glycosylation, phosphorylation were analysed.
The isoleucine to threonine substitution is known to impact post translation modifications such as phosphorylation.
RIG-I activation is tightly regulated by post-translational modifications, such as polyubiquitination and phosphorylation.
Other modifications such as glycosylation are possible, although tyrosine glycosylation is believed to be rare [44].
This change in microtubules requires the participation of enzymes that reverse tubulin modifications, such as acetylation.
Perhaps CtrIncA requires post-translational modifications such as phosphorylation, to become fusogenic [32].
In addition intracellular HSF1 undergoes other modifications such as sumoylation and acetylation after stress [17].
The latter includes histone modifications such as deacetylation [1], acetylation [2], and methylation [3].
The Protein Pilot™ algorithm was selected to search automatically for biological modifications such as homocysteines.
Similar to other covalent modifications, such as phosphorylation or methylation, ubiquitination is reversible.
In addition to active marks, there are negative methyl modifications, such as H4K20me3.
